4ZM4
Complex structure of PctV K276R mutant with PMP and 3-dehydroshkimate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0008483 | molecular_function | transaminase activity |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0008483 | molecular_function | transaminase activity |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | SER119 |
| A | HOH623 |
| A | HOH652 |
| B | GLY306 |
| B | VAL307 |
| A | GLY120 |
| A | THR121 |
| A | TYR147 |
| A | ASN220 |
| A | ASP248 |
| A | VAL250 |
| A | ILE251 |
| A | ARG276 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue P3B B 501 |
| Chain | Residue |
| A | GLY306 |
| A | VAL307 |
| A | HOH619 |
| B | SER28 |
| B | ARG31 |
| B | TYR64 |
| B | SER119 |
| B | GLY120 |
| B | THR121 |
| B | TYR147 |
| B | GLY149 |
| B | ASN220 |
| B | ASP248 |
| B | VAL250 |
| B | ILE251 |
| B | ARG276 |
| B | GLU416 |
| B | HOH629 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue PLP C 501 |
| Chain | Residue |
| C | SER119 |
| C | GLY120 |
| C | THR121 |
| C | TYR147 |
| C | GLY149 |
| C | GLU215 |
| C | ASN220 |
| C | ASP248 |
| C | VAL250 |
| C | ILE251 |
| C | ARG276 |
| C | HOH626 |
| D | GLY306 |
| D | VAL307 |
| D | HOH624 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue PLP D 501 |
| Chain | Residue |
| C | GLY306 |
| C | VAL307 |
| D | SER119 |
| D | GLY120 |
| D | THR121 |
| D | TYR147 |
| D | HIS148 |
| D | GLY149 |
| D | ASN220 |
| D | ASP248 |
| D | VAL250 |
| D | ILE251 |
| D | ARG276 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue P3B E 501 |
| Chain | Residue |
| E | SER28 |
| E | ARG31 |
| E | TYR64 |
| E | SER119 |
| E | GLY120 |
| E | THR121 |
| E | TYR147 |
| E | GLY149 |
| E | ASN220 |
| E | ASP248 |
| E | VAL250 |
| E | ILE251 |
| E | ARG276 |
| E | GLU416 |
| E | HOH601 |
| E | HOH620 |
| E | HOH622 |
| E | HOH625 |
| E | HOH657 |
| F | GLY306 |
| F | VAL307 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue PLP F 501 |
| Chain | Residue |
| E | GLY306 |
| E | VAL307 |
| F | SER119 |
| F | GLY120 |
| F | THR121 |
| F | TYR147 |
| F | GLY149 |
| F | ASN220 |
| F | ASP248 |
| F | VAL250 |
| F | ILE251 |
| F | ARG276 |
| F | HOH619 |
| F | HOH623 |
